Abstract
Original language | English |
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Journal | Biomacromolecules |
Volume | 19 |
Pages (from-to) | 2905-2912 |
ISSN | 1525-7797 |
DOIs | |
Publication status | Published - 2018 |
Cite this
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Revealing the Dimeric Crystal and Solution Structure of β-Lactoglobulin at pH 4 and Its pH and Salt Dependent Monomer–Dimer Equilibrium. / Khan, Sanaullah; Ipsen, Richard; Almdal, Kristoffer; Svensson, Birte; Harris, Pernille.
In: Biomacromolecules, Vol. 19, 2018, p. 2905-2912.Research output: Contribution to journal › Journal article › Research › peer-review
TY - JOUR
T1 - Revealing the Dimeric Crystal and Solution Structure of β-Lactoglobulin at pH 4 and Its pH and Salt Dependent Monomer–Dimer Equilibrium
AU - Khan, Sanaullah
AU - Ipsen, Richard
AU - Almdal, Kristoffer
AU - Svensson, Birte
AU - Harris, Pernille
PY - 2018
Y1 - 2018
N2 - The dimeric structure of bovine β-lactoglobulin A (BLGA) at pH 4.0 was solved to 2.0 Å resolution. Fitting the BLGA pH 4.0 structure to SAXS data at low ionic strength (goodness of fit R-factor = 3.6%) verified the dimeric state in solution. Analysis of the monomer–dimer equilibrium at varying pH and ionic strength by SAXS and scattering modeling showed that BLGA is dimeric at pH 3.0 and 4.0, shifting toward a monomer at pH 2.2, 2.6, and 7.0 yielding monomer/dimer ratios of 80/20%, 50/50%, and 25/75%, respectively. BLGA remained a dimer at pH 3.0 and 4.0 in 50–150 mM NaCl, whereas the electrostatic shielding raised the dimer content at pH 2.2, 2.6, and 7.0, i.e., below and above the pI. Overall, the findings provide new insights into the molecular characteristics of BLGA relevant for dairy product formulations and for various biotechnological and pharmaceutical applications.
AB - The dimeric structure of bovine β-lactoglobulin A (BLGA) at pH 4.0 was solved to 2.0 Å resolution. Fitting the BLGA pH 4.0 structure to SAXS data at low ionic strength (goodness of fit R-factor = 3.6%) verified the dimeric state in solution. Analysis of the monomer–dimer equilibrium at varying pH and ionic strength by SAXS and scattering modeling showed that BLGA is dimeric at pH 3.0 and 4.0, shifting toward a monomer at pH 2.2, 2.6, and 7.0 yielding monomer/dimer ratios of 80/20%, 50/50%, and 25/75%, respectively. BLGA remained a dimer at pH 3.0 and 4.0 in 50–150 mM NaCl, whereas the electrostatic shielding raised the dimer content at pH 2.2, 2.6, and 7.0, i.e., below and above the pI. Overall, the findings provide new insights into the molecular characteristics of BLGA relevant for dairy product formulations and for various biotechnological and pharmaceutical applications.
U2 - 10.1021/acs.biomac.8b00471
DO - 10.1021/acs.biomac.8b00471
M3 - Journal article
VL - 19
SP - 2905
EP - 2912
JO - Biomacromolecules
JF - Biomacromolecules
SN - 1525-7797
ER -